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Database: UniProt
Entry: A0A1Q9K2K7_9FIRM
LinkDB: A0A1Q9K2K7_9FIRM
Original site: A0A1Q9K2K7_9FIRM 
ID   A0A1Q9K2K7_9FIRM        Unreviewed;       679 AA.
AC   A0A1Q9K2K7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Transcriptional antiterminator {ECO:0000313|EMBL:OLR62820.1};
GN   ORFNames=BHF69_09070 {ECO:0000313|EMBL:OLR62820.1};
OS   Anaerostipes sp. 992a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Anaerostipes.
OX   NCBI_TaxID=1261637 {ECO:0000313|EMBL:OLR62820.1, ECO:0000313|Proteomes:UP000187371};
RN   [1] {ECO:0000313|EMBL:OLR62820.1, ECO:0000313|Proteomes:UP000187371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=992a {ECO:0000313|EMBL:OLR62820.1,
RC   ECO:0000313|Proteomes:UP000187371};
RX   PubMed=27613689;
RA   Trachsel J., Bayles D.O., Looft T., Levine U.Y., Allen H.K.;
RT   "Function and Phylogeny of Bacterial Butyryl Coenzyme A:Acetate
RT   Transferases and Their Diversity in the Proximal Colon of Swine.";
RL   Appl. Environ. Microbiol. 82:6788-6798(2016).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OLR62820.1}.
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DR   EMBL; MJIG01000004; OLR62820.1; -; Genomic_DNA.
DR   RefSeq; WP_075670879.1; NZ_MJIG01000004.1.
DR   AlphaFoldDB; A0A1Q9K2K7; -.
DR   STRING; 1261637.BHF69_09070; -.
DR   OrthoDB; 3175596at2; -.
DR   Proteomes; UP000187371; Unassembled WGS sequence.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd05568; PTS_IIB_bgl_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 1.10.1790.10; PRD domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR007737; Mga_HTH.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR30185; CRYPTIC BETA-GLUCOSIDE BGL OPERON ANTITERMINATOR; 1.
DR   PANTHER; PTHR30185:SF18; TRANSCRIPTIONAL REGULATOR MTLR; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   Pfam; PF05043; Mga; 1.
DR   Pfam; PF00874; PRD; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   SUPFAM; SSF63520; PTS-regulatory domain, PRD; 1.
DR   PROSITE; PS51372; PRD_2; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000187371};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          286..393
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          397..483
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          533..678
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   679 AA;  79021 MW;  6D0AF4C93F3D8747 CRC64;
     MSIIYNLDVR CYEILNYLLY QDGYTTVVQL AEEKGISKRS VYYDIRKINE WLEAQELTPL
     EIERKKGIWI DEEQKTLIRT KLKMIPPKLA YVFTPVERIK IIICSILQRN RNLFLDDFME
     LCQVSRNTTI NDMKEAGKVI SEYQLQLIYE NGKGYHIVGD LVRKRSIYFA YFSSIADFYK
     KEILPLDDPE KVQQIIEKLK DIENALDVQY VQGTLYTIAV FFSTIDNRTD ILEFSEDEKS
     EIMYTKEYEM VSKRFEELDE SERLYLALHL LGSRIQSIPV DFMNEKTGQE TQKLSRILVE
     AFSRITGIGF SKEDELVQAI AAHLKTSLYR YRYGVQLANP MLDNIKSEYG DLFEVTARAC
     KYLEKEIGVP IPDGEIAYLT LHFGAFITSG QQQEEQLRVL IVCPNGLSTA NMIRGEIKTL
     VPNAETVDIR SLKDYQKQHN YNVVISTVVI EEEKNLILVH PILTDNDRMT VLKKCMKYEY
     SNHVNITQIT EIASKYMTEK NLKEFKAELM EHFSKTSLKK YVKRGSSQKG IQEMLQKSYI
     HIVKDSMPWE NAVQISGETL LNEKFIKQSY IDSIIQKTKQ YGPYMFITKH VFLAHSEIEH
     GANKMGIELT VFKKPIEFTA LDGKKRYAKI ILTLSAQDHK AHIRLLNDIM TIFSESENEE
     MIWKSETAEN IKNMICQLL
//
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